Literature DB >> 6281205

beta-Endorphin. Circular dichroism of synthetic human analogs with various chain lengths in methanol solutions.

M D Jibson, C H Li.   

Abstract

The alpha-helix content of human beta-endorphin (beta h-EP) has been determined by circular dichroism (CD) in solutions ranging from 0 to 95% methanol in water. In addition, the CD spectra of beta h-EP-(1-30),-(1-29),-(1-28),-(1-27),-(1-26),-(1-21) and -(1-15) have been examined in 90% methanol, and their alpha-helix contents estimated using parameters determined for this solvent. Addition of methanol to beta h-EP solutions brings about a noncooperative formation of alpha-helix. An attempt to correlate secondary structure in methanol with biological and immunological activities showed limited direct correspondence, but may indicate the involvement of the tertiary interactions.

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Year:  1981        PMID: 6281205

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  1 in total

1.  Purification and characterization of recombinant Rev protein of human immunodeficiency virus type 1.

Authors:  C M Nalin; R D Purcell; D Antelman; D Mueller; L Tomchak; B Wegrzynski; E McCarney; V Toome; R Kramer; M C Hsu
Journal:  Proc Natl Acad Sci U S A       Date:  1990-10       Impact factor: 11.205

  1 in total

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